ArticleProceedings of the National Academy of Sciences of the United States of America1988
Human 67-kDa calelectrin contains a duplication of four repeats found in 35-kDa lipocortins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 109 citations in OpenAlex.
- Structure of the human annexin VI gene.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kinase C.The Journal of cell biology · 1991Article
- Protein-synthesis-dependent induction of annexin I by glucocorticoid.The Biochemical journal · 1991Article
- Expression of annexin VI (p68, 67 kDa-calelectrin) in normal human tissues: evidence for developmental regulation in B- and T-lymphocytes.Histochemistry · 1991Article
- Annexins: calcium-binding proteins of multi-functional importance?Medical microbiology and immunology · 1991Review
- Purification and partial sequence analysis of plant annexins.The Biochemical journal · 1990Article
- Monoclonal antibodies specific to a Ca2(+)-bound form of lipocortin I distinguish its Ca2(+)-dependent phospholipid-binding ability from its ability to inhibit phospholipase A2.The Biochemical journal · 1990Article
- Synexin (annexin VII): a cytosolic calcium-binding protein which promotes membrane fusion and forms calcium channels in artificial bilayer and natural membranes.The Journal of membrane biology · 1990Review
- Molecular mechanisms of calcium-induced membrane fusion.Journal of bioenergetics and biomembranes · 1990Review
- Identification of the 32 kDa components of bovine lens EDTA-extractable protein as endonexins I and II.The Biochemical journal · 1990Article
- Characterization of Ca2(+)-dependent phospholipid binding, vesicle aggregation and membrane fusion by annexins.The Biochemical journal · 1990Article
- Calcium-binding proteins 33 kDa, 35 kDa, and 65/67 kDa in normal rat and Morris hepatoma tissues. A biochemical and immunohistochemical study.Histochemistry · 1990Article
- A dimeric form of lipocortin-1 in human placenta.The Biochemical journal · 1989Article
- Purification and spectral studies on the Ca2+-binding properties of 67 kDa calcimedin.The Biochemical journal · 1989Article
- Calcium channel activity of purified human synexin and structure of the human synexin gene.Proceedings of the National Academy of Sciences of the United States of America · 1989Article
- Phospholipase A2--regulation and inhibition.Klinische Wochenschrift · 1989Article
- The structure of cytochrome b561, a secretory vesicle-specific electron transport protein.The EMBO journal · 1988Article
- p36, the major cytoplasmic substrate of src tyrosine protein kinase, binds to its p11 regulatory subunit via a short amino-terminal amphiphatic helix.The EMBO journal · 1988Article
- Biosynthesis, secretion and extracellular localization of anchorin CII, a collagen-binding protein of the calpactin family.The EMBO journal · 1988Article
- Functional and genetic analysis of annexin VI.Molecular and cellular biochemistryReview
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5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 67-kDa calelectrin is the largest member of a family of Ca2+-binding proteins that associate with membranes and phospholipids in a Ca2+-dependent manner. Oligonucleotide probes based on peptide sequences obtained from purified bovine 67-kDa calelectrin were used to screen a human retina cDNA library, and the complete primary structure of human 67-kDa calelectrin was deduced by DNA sequence analysis. The protein consists of eight 68-amino acid repeats separated by linking sequences of variable lengths. It is highly similar to the human lipocortin I and II sequences, each of which contains four such repeats. The amino termini of the three proteins show no sequence similarity; however, in the repeated regions the proteins are 42-45% identical in sequence. Analysis of the 16 repeats from the three proteins provides insights into the structural basis for Ca2+-dependent phospholipid binding. These data place the calelectrins and the lipocortins into the same gene family and suggest that these proteins have similar functions and have evolved from a common ancestor.
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